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eNOS (Ser-1177), Phosphospecific Antibody

Applications

  • WB

Reactivity

  • Human
  • Mouse
  • Rat
Overview
Catalog # bs-70573R
Product Name eNOS (Ser-1177), Phosphospecific Antibody
Applications WB
Specificity The antibody detects a 140 kDa* band corresponding to eNOS on SDS-PAGE immunoblots of human umbilical vein endothelial cells grown normally or treated with calyculin A. This reactivity is not observed after lambda phosphatase treatment.
Reactivity Human, Mouse, Rat
Specifications
Conjugation Unconjugated
Host Rabbit
Source Phospho-eNOS (Ser-1177) synthetic peptide (coupled to carrier protein) corresponds to amino acids surrounding Ser-1177 in human eNOS. This sequence is conserved in rat and mouse eNOS.
Modification Site Ser-1177
Clonality Polyclonal
Isotype IgG
Concentration Lot dependent
Purification Antigen Affinity purification
Storage Buffer PBS + 1 mg/ml BSA, 0.05% NaN3 and 50% glycerol
Storage Condition Storage at -20°C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20°C.
Target
Swiss Prot P29474
Synonyms endothelial Nitric Oxide Synthase, eNOS, ecNOS, NOS-III, NOS3, NOSIII
Background Nitric oxide (NO) has a broad range of biological activities and is implicated in signaling pathways in phylogenetically diverse species. Nitric oxide synthases (NOS), the enzymes responsible for synthesis of NO, are homodimers whose monomers are themselves two fused enzymes: a cytochrome reductase and a cytochrome that requires three cosubstrates (L-arginine, NADPH, and oxygen) and five cofactors or prosthetic groups (FAD, FMN, calmodulin, tetrahydrobiopterin, and heme). Several distinct NOS isoforms are produced from three distinct genes. The inducible form of NOS, iNOS (NOS-II), is Ca2+ independent and is expressed in a broad range of cell types, and two constitutive Ca2+/CaM-dependent forms of NOS: nNOS (bNOS, NOS-I) identified in neurons and eNOS (ecNOS, NOS-III) identified in endothelial cells. Regulation of eNOS activity occurs through phosphorylation at multiple sites. Phosphorylation of Ser-633 (mouse Ser-632) in the FMN binding domain increases eNOS activity and may be important for the maintenance of NO synthesis after initial activation by Ca2+ flux and Ser-1177 phosphorylation.
Application Dilution
WB 1:300-5000